Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis

Yu Xia; Hao Zhang; Jianxin Zhao; Fengwei Tian; Wei Chen

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Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis

Yu Xia,Hao Zhang,Jianxin Zhao,Fengwei Tian,Wei Chen * #

School of Food Science and Technology, Jiangnan University

*Correspondence author

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Funding: 教育部博士点基金,国家自然科学基金,科技部863项目（No.20050295003,30670065,2006AA10Z318）

Opened online:29 December 2008

Accepted by: none

Citation: Yu Xia,Hao Zhang,Jianxin Zhao.Secretion of a heterologous cytoplasmic b-galactosidase in Bacillus subtilis[OL]. [29 December 2008] http://en.paper.edu.cn/en_releasepaper/content/27070

A cytoplasmic b-galactosidase (BgaB) from Geobacillus stearothermophilus IAM11001, which can not be secreted in Bacillus subtilis by mediation of two general secretory signal peptides, was secreted in Bacillus subtilis when it was fused to a twin-arginine signal peptide. The extracellular BgaB enzymatic activity accounted for about 39% of the total enzymatic activity at 18 h of cultivation in Luria-Bertani medium. As a control of secretion, the extracellular BgaB enzymatic activity obtained at the same time of cultivation accounted for less than 3% of the total enzymatic activity when the signal peptide coding sequence was absent from the N-terminus of the target gene bgaB.

Keywords:Bacillus subtilis;protein secretion;b-galactosidase; twin-arginine translocation;signal peptide;enzymatic activity

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